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Q28178 (TSP1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Thrombospondin-1
Gene names
Name:THBS1
Synonyms:TSP-1, TSP1
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length1170 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions. Ligand for CD36 mediating antiangiogenic properties By similarity. May play a role in dentinogenesis and/or maintenance of dentin and dental pulp. Ref.1

Subunit structure

Homotrimer; disulfide-linked By similarity. Can bind to fibrinogen, fibronectin, laminin, type V collagen and integrins alpha-V/beta-1, alpha-V/beta-3 and alpha-IIb/beta-3. Binds heparin. Interacts (via the TSP type I repeats) with CD36; the interaction conveys an antiangiogenic effect. Interacts (via the TSP type I repeats) with HRG; the interaction blocks the antiangiogenic effect of THBS1 with CD36 By similarity.

Tissue specificity

Odontoblasts. Ref.1

Sequence similarities

Belongs to the thrombospondin family.

Contains 2 EGF-like domains.

Contains 1 laminin G-like domain.

Contains 1 TSP C-terminal (TSPC) domain.

Contains 3 TSP type-1 domains.

Contains 8 TSP type-3 repeats.

Contains 1 VWFC domain.

Ontologies

Keywords
   Biological processCell adhesion
   DomainEGF-like domain
Repeat
Signal
   LigandCalcium
Heparin-binding
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: InterPro

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

heparin binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 By similarity
Chain19 – 11701152Thrombospondin-1
PRO_0000035841

Regions

Domain65 – 270206Laminin G-like
Domain316 – 37358VWFC
Domain379 – 42951TSP type-1 1
Domain435 – 49056TSP type-1 2
Domain492 – 54756TSP type-1 3
Domain547 – 58741EGF-like 1
Domain646 – 69045EGF-like 2
Repeat691 – 72636TSP type-3 1
Repeat727 – 76236TSP type-3 2
Repeat763 – 78523TSP type-3 3
Repeat786 – 82136TSP type-3 4
Repeat822 – 84423TSP type-3 5
Repeat845 – 88238TSP type-3 6
Repeat883 – 91836TSP type-3 7
Repeat919 – 95436TSP type-3 8
Domain958 – 1170213TSP C-terminal
Region47 – 9549Heparin-binding By similarity
Motif926 – 9283Cell attachment site Potential

Amino acid modifications

Glycosylation2481N-linked (GlcNAc...) Potential
Glycosylation3601N-linked (GlcNAc...) Potential
Glycosylation7081N-linked (GlcNAc...) Potential
Glycosylation10671N-linked (GlcNAc...) Potential
Glycosylation10851N-linked (GlcNAc...) Potential
Disulfide bond171 ↔ 232 By similarity
Disulfide bond270Interchain Probable
Disulfide bond274Interchain Probable
Disulfide bond391 ↔ 423 By similarity
Disulfide bond395 ↔ 428 By similarity
Disulfide bond406 ↔ 413 By similarity
Disulfide bond447 ↔ 484 By similarity
Disulfide bond451 ↔ 489 By similarity
Disulfide bond462 ↔ 474 By similarity
Disulfide bond504 ↔ 541 By similarity
Disulfide bond508 ↔ 546 By similarity
Disulfide bond519 ↔ 531 By similarity
Disulfide bond551 ↔ 562 By similarity
Disulfide bond556 ↔ 572 By similarity
Disulfide bond575 ↔ 586 By similarity
Disulfide bond592 ↔ 608 By similarity
Disulfide bond599 ↔ 617 By similarity
Disulfide bond620 ↔ 644 By similarity
Disulfide bond650 ↔ 663 By similarity
Disulfide bond657 ↔ 676 By similarity
Disulfide bond678 ↔ 689 By similarity
Disulfide bond705 ↔ 713 By similarity
Disulfide bond718 ↔ 738 By similarity
Disulfide bond754 ↔ 774 By similarity
Disulfide bond777 ↔ 797 By similarity
Disulfide bond813 ↔ 833 By similarity
Disulfide bond836 ↔ 856 By similarity
Disulfide bond874 ↔ 894 By similarity
Disulfide bond910 ↔ 930 By similarity
Disulfide bond946 ↔ 1167 By similarity

Experimental info

Sequence conflict8051S → G in CAA60950. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q28178 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: 0DD6ADF3E5FA031A

FASTA1,170129,534
        10         20         30         40         50         60 
MGLAWGLGVL LLLHACGSNR IPESGGDNSV FDIFELTGAA RKRSGRRLVK GPDPSSPAFR 

        70         80         90        100        110        120 
IEDANLIPPV PDKKFQDLVD AVRAEKGFLL LASLRQMKKT RGTLLAVERK DHSGQVFSVI 

       130        140        150        160        170        180 
SNGKAGTLDL SLTVQGKQHV VSVEEALLAT GQWKSITLFV QEDRAQLYID CEKMENAELD 

       190        200        210        220        230        240 
VPIQSIFTRD LASIARLRIA KGGVNDNFQG VLQNVRFVFG TTPEDILRNK GCSSSTSVFV 

       250        260        270        280        290        300 
TLDNNVVNGS SPAIRTDYIG HKTKDLQAIC GISCDELSSM VLELRGLRTI VTTLQDSIRK 

       310        320        330        340        350        360 
VTEENKELAN ELRRPPLCYH NGVQYRTGDE WTVDSCTECR CQNSVTICKK VSCPIMPCSN 

       370        380        390        400        410        420 
ATVPDGECCP RCWPSDSADD GWSPWSEWTS CSVTCGNGIQ QRGRSCDSLN NRCEGSSVQT 

       430        440        450        460        470        480 
RTCHIQECDK RFKQDGGWSH WSPWSSCSVT CGDGVITRIR LCNSPSPQMN GKPCEGKARE 

       490        500        510        520        530        540 
TKACQKDSCP INGGWGPWSP WDICSVTCGG GVQKRSRLCN NPKPQFGGKD CVGDVTENQI 

       550        560        570        580        590        600 
CNKQDCPIDG CLSNPCFAGV QCTSYPDGSW KCGACPPGYS GDGVECKDVD ECKEVPDACF 

       610        620        630        640        650        660 
NHNGEHRCEN TDPGYNCLPC PPRFTGSQPF GRGVEHATAN KQVCKPRNPC TDGTHDCNKN 

       670        680        690        700        710        720 
AKCNYLGHYS DPMYRCECKP GYAGNGIICG EDTDLDGWPN EDLLCVANAT YHCRKDNCPN 

       730        740        750        760        770        780 
LPNSGQEDYD KDGIGDACDD DDDNDKIPDD RDNCPFHYNP AQYDYDRDDV GDRCDNCPYN 

       790        800        810        820        830        840 
HNPDQADTDN NGEGDACAAD IDGDSILNER DNCQYVYNVD QKDTDMDGVG DQCDNCPLEH 

       850        860        870        880        890        900 
NPDQLDSDSD RIGDTCDNNQ DIDEDGHQNN LDNCPYVPNA NQADHDKDGK GDACDHDDDN 

       910        920        930        940        950        960 
DGIPDDRDNC RLVPNPDQKD SDGDGRGDAC KDDFDQDKVP DIDDICPENV DISETDFRRF 

       970        980        990       1000       1010       1020 
QMIPLDPKGT SQNDPNWVVR HQGKELVQTV NCDPGLAVGY DEFNAVDFSG TFFINTERDD 

      1030       1040       1050       1060       1070       1080 
DYAGFVFGYQ SSSRFYVVMW KQVTQSYWDT NPTRAQGYSG LSVKVVNSTT GPGEHLRNAL 

      1090       1100       1110       1120       1130       1140 
WHTGNTSGQV RTLWHDPRHI GWKDFTAYRW HLSHRPKTGF IRVVMYEGKK IMADSGPIYD 

      1150       1160       1170 
KTYAGGRLGL FVFSQEMVFF SDLKYECRDS

« Hide

References

[1]"cDNA cloning of bovine thrombospondin 1 and its expression in odontoblasts and predentin."
Ueno A., Yamashita K., Nagata T., Tsurumi C., Miwa Y., Kitamura S., Inoue H.
Biochim. Biophys. Acta 1382:17-22(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], POSSIBLE FUNCTION, TISSUE SPECIFICITY.
Strain: Holstein.
Tissue: Tooth.
[2]"Cloning and sequencing of bovine thrombospondin stimulatory effect of TGF-beta."
Zafar R.S., Moll Y.D., Womack J.F., Walz D.A.
Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-18 AND 710-1170.
Tissue: Aortic endothelium.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB005287 mRNA. Translation: BAA21115.1.
X87618 mRNA. Translation: CAA60950.1.
X87619 mRNA. Translation: CAA60951.1.
IPIIPI00712084.
PIRS55501.
RefSeqNP_776621.1. NM_174196.1.
UniGeneBt.109568.

3D structure databases

ProteinModelPortalQ28178.
SMRQ28178. Positions 25-233, 434-546, 549-1169.
ModBaseSearch...

Protein-protein interaction databases

IntActQ28178. 1 interaction.

PTM databases

GlycoSuiteDBQ28178.

Proteomic databases

PaxDbQ28178.
PRIDEQ28178.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID281530.
KEGGbta:281530.

Organism-specific databases

CTD7057.

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000007542.
HOVERGENHBG018006.
InParanoidQ28178.
KOK16857.
OrthoDBEOG466VK5.

Family and domain databases

Gene3D2.60.120.200. 2 hits.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd.
IPR013032. EGF-like_CS.
IPR001791. Laminin_G.
IPR000884. Thrombospondin_1_rpt.
IPR003367. Thrombospondin_3-like_rpt.
IPR017897. Thrombospondin_3_rpt.
IPR008859. Thrombospondin_C.
IPR001007. VWF_C.
[Graphical view]
PfamPF07645. EGF_CA. 1 hit.
PF00090. TSP_1. 3 hits.
PF02412. TSP_3. 7 hits.
PF05735. TSP_C. 1 hit.
PF00093. VWC. 1 hit.
[Graphical view]
SMARTSM00181. EGF. 3 hits.
SM00209. TSP1. 3 hits.
SM00210. TSPN. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
SUPFAMSSF49899. ConA_like_lec_gl. 2 hits.
SSF82895. TSP1. 3 hits.
PROSITEPS00022. EGF_1. False negative.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 2 hits.
PS50025. LAM_G_DOMAIN. False negative.
PS50092. TSP1. 3 hits.
PS51234. TSP3. 8 hits.
PS51236. TSP_CTER. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20805487.

Entry information

Entry nameTSP1_BOVIN
AccessionPrimary (citable) accession number: Q28178
Secondary accession number(s): Q28179
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 1, 2000
Last modified: May 1, 2013
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents